Structure of the transmembrane region of the M2 protein H+ channel

Protein Science - Tập 10 Số 11 - Trang 2241-2250 - 2001
Junfeng Wang1,2, Sanguk Kim1,2, Frank Kovacs1,2, Timothy A. Cross3,1,2
1Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32310 USA
2. The National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida 32310, USA
3Department of Chemistry, Florida State University, Tallahassee, Florida 32310, USA

Tóm tắt

AbstractThe transmembrane domain of the M2 protein from influenza A virus forms a nearly uniform and ideal helix in a liquid crystalline bilayer environment. The exposure of the hydrophilic backbone structure is minimized through uniform hydrogen bond geometry imposed by the low dielectric lipid environment. A high‐resolution structure of the monomer backbone and a detailed description of its orientation with respect to the bilayer were achieved using orientational restraints from solid‐state NMR. With this unique information, the tetrameric structure of this H+ channel is constrained substantially. Features of numerous published models are discussed in light of the experimental structure of the monomer and derived features of the tetrameric bundle.

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